Tämä ubikitiinigeeni koodaa fuusioproteiinia, jonka N-terminaalissa on yksi ubikitiini-alue ja C-terminaalissa ribosomaalinen proteiini S27a. Hiivassa tämä konservoitunut geeni tuottaa vapaan monoubikitiinin ja ribosomaalisen proteiinin S27a. ( S27a on komponettina ribosomin 40S alayksikössä). Tässä prekursoriproteiinissa on useita asetyloituneita lysiinejä C-terminaalisessa jaksossa. Kuvassa ylin on tämän UBA80 kaava.
https://www.researchgate.net/profile/Choongseob_Oh/publication/256489807/figure/fig1/AS:213970884534276@1428026042193/a-Schematic-representation-of-the-4Ub-genes-Rps27a-and-Uba52-encode-Ub-as-a-fusion.png
PubMeD lähde käyttää mieluiten geeninimeä RPS27A, ( mikä on ymmärrettävää, että ei tule sekaannusta, koska tässä järejstelmsäsä on tosiaan paljon näitä UB nimiä)
https://www.ncbi.nlm.nih.gov/gene/6233
- also known as
- UBC; S27A; CEP80; UBA80; HEL112; UBCEP1; UBCEP80
- Summary
- Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein.
- This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus.
- When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm.
- Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.[provided by RefSeq, Sep 2008]
- Expression
- Ubiquitous expression in ovary (RPKM 575.2), lymph node (RPKM 347.6) and 25 other tissues See more
- Orthologs
- mouse
all
- Preferred Names
- ubiquitin-40S ribosomal protein S27a
- Names
- 40S ribosomal protein S27a
- epididymis luminal protein 112
- ubiquitin C
- ubiquitin and ribosomal protein S27a
- ubiquitin carboxyl extension protein 80
- ubiquitin-CEP80
- Conserved Domains (2) summary
-
- cd01803
Location:1 → 76 - Ubiquitin; Ubiquitin
- pfam01599
Location:103 → 147 - Ribosomal_S27; Ribosomal protein S27a
- cd01803
https://www.ncbi.nlm.nih.gov/protein/NP_001129064.1
Related articles in PubMed
- Identification and expression of MMSA-8, and its clinical significance in multiple myeloma. He R, et al. Oncol Rep, 2017 Jun. PMID 28498418, Free PMC Article
- RPS27a promotes proliferation, regulates cell cycle progression and inhibits apoptosis of leukemia cells. Wang H, et al. Biochem Biophys Res Commun, 2014 Apr 18. PMID 24680683
- A novel component of the ubiquitin pathway, ubiquitin carboxyl extension protein 1 is overexpressed in prostate cancer. Ko Y, et al. Int J Mol Med, 2005 Feb. PMID 15647830
- Structure and properties of a dimeric N-terminal fragment of human ubiquitin. Bolton D, et al. J Mol Biol, 2001 Dec 7. PMID 11733996
- Identification of the long ubiquitin extension as ribosomal protein S27a. Redman KL, et al. Nature, 1989 Mar 30. PMID 2538756
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
- the full-length cDNA sequence of MMSA-8 was cloned in MM and it was hypothesized that MMSA-8 is MM-associated RPS27A transcript variant 1
- RPS27a enhances viral LMP1-mediated proliferation and invasion, suggesting that RPS27a interacts with LMP1 and stabilizes it by suppressing proteasome-mediated ubiquitination.
- Imatinib-resistant K562/G01 cells expressed significantly higher levels of STAT3 and RPS27a compared with those of K562 cells.
- RPS27A expression was found to have a weak inverse correlation with overexpression of multifunctional protein YB-1 in HCC tissues.
- RPS27a appears to be a novel stress sensor in the cell which amplifies p53 response to arrest cell cycle....The small ribosomal protein RPS27a is known to play a role in the activation of cellular checkpoints via p53 which links ribosome biogenesis to cell cycle progression. Here, we show that RPS27a gene is a direct transcriptional target of p53 and is overexpressed in response to DNA damage. Elevated RPS27a level was associated with increased expression of p53 and its target p21(Waf1) gene. The RPS27a activity was specifically inhibited in the presence of a dominant negative mutant of p53. Down-regulation of ectopically expressed RPS27a by RNA interference blocked the activation of p21(waf1) in response to DNA damage. Thus, RPS27a appears to be a novel stress sensor in the cell which amplifies p53 response to arrest cell cycle.
- Knockdown of RPS27a inhibits the proliferation, induces cell cycle arrest and potentiates the effect of imatinib on apoptosis of K562 cells.
- Gene expression profiles showed that RPS27A was down-regulated in epidermolysis bullosa subtypes.
- S27a plays a non-redundant role in mediating p53 activation in response to ribosomal stress via interplaying with MDM2.
- ubiquitin carboxyl extension protein 1 is overexpressed in prostate cancer
